메뉴 건너뛰기




Volumn 71, Issue 8, 2014, Pages 447-463

Non-muscle myosins in tumor progression, cancer cell invasion, and metastasis

Author keywords

Actin; Cancer; Metastasis; Myosin

Indexed keywords

MYOSIN; MYOSIN 1A; MYOSIN 1E; MYOSIN 1F; MYOSIN I; MYOSIN II; MYOSIN IIA; MYOSIN IX; MYOSIN VI; MYOSIN VII; MYOSIN X; MYOSIN XVIII; NON MUSCLE MYOSIN; PROTEIN P53; UNCLASSIFIED DRUG; ACTIN;

EID: 84908051092     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.21187     Document Type: Review
Times cited : (81)

References (154)
  • 1
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams JM, Cory S. 2007. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 26(9):1324-1337.
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 2
    • 84892834113 scopus 로고    scopus 로고
    • Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer
    • Aguilar-Cuenca R, Juanes-Garcia A, Vicente-Manzanares M. 2014. Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer. Cell Mol Life Sci 71(3):479-492.
    • (2014) Cell Mol Life Sci , vol.71 , Issue.3 , pp. 479-492
    • Aguilar-Cuenca, R.1    Juanes-Garcia, A.2    Vicente-Manzanares, M.3
  • 5
    • 79959954909 scopus 로고    scopus 로고
    • Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network
    • Almeida CG, Yamada A, Tenza D, Louvard D, Raposo G, Coudrier E. 2011. Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network. Nat Cell Biol 13(7):779-789.
    • (2011) Nat Cell Biol , vol.13 , Issue.7 , pp. 779-789
    • Almeida, C.G.1    Yamada, A.2    Tenza, D.3    Louvard, D.4    Raposo, G.5    Coudrier, E.6
  • 6
    • 80053444351 scopus 로고    scopus 로고
    • Filopodia and adhesion in cancer cell motility
    • Arjonen A, Kaukonen R, Ivaska J. 2011. Filopodia and adhesion in cancer cell motility. Cell Adh Migr 5(5):421-430.
    • (2011) Cell Adh Migr , vol.5 , Issue.5 , pp. 421-430
    • Arjonen, A.1    Kaukonen, R.2    Ivaska, J.3
  • 10
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
    • Berg JS, Derfler BH, Pennisi CM, Corey DP, Cheney RE. 2000. Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J Cell Sci 113(Pt 19):3439-3451.
    • (2000) J Cell Sci , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 12
    • 84882630671 scopus 로고    scopus 로고
    • Telomerase at the intersection of cancer and aging
    • Bernardes de Jesus B, Blasco MA. 2013. Telomerase at the intersection of cancer and aging. Trends Genet 29(9):513-520.
    • (2013) Trends Genet , vol.29 , Issue.9 , pp. 513-520
    • Bernardes de Jesus, B.1    Blasco, M.A.2
  • 13
    • 84881641667 scopus 로고    scopus 로고
    • Myosin 1e is a component of the glomerular slit diaphragm complex that regulates actin reorganization during cell-cell contact formation in podocytes
    • Bi J, Chase SE, Pellenz CD, Kurihara H, Fanning AS, Krendel M. 2013. Myosin 1e is a component of the glomerular slit diaphragm complex that regulates actin reorganization during cell-cell contact formation in podocytes. Am J Physiol Renal Physiol 305(4):F532-F544.
    • (2013) Am J Physiol Renal Physiol , vol.305 , Issue.4 , pp. F532-F544
    • Bi, J.1    Chase, S.E.2    Pellenz, C.D.3    Kurihara, H.4    Fanning, A.S.5    Krendel, M.6
  • 14
    • 84887830790 scopus 로고    scopus 로고
    • Characterization of three full-length human nonmuscle myosin II paralogs
    • Billington N, Wang A, Mao J, Adelstein RS, Sellers JR. 2013. Characterization of three full-length human nonmuscle myosin II paralogs. J Biol Chem 288(46):33398-33410.
    • (2013) J Biol Chem , vol.288 , Issue.46 , pp. 33398-33410
    • Billington, N.1    Wang, A.2    Mao, J.3    Adelstein, R.S.4    Sellers, J.R.5
  • 15
    • 33747622327 scopus 로고    scopus 로고
    • Myosin-X is a molecular motor that functions in filopodia formation
    • Bohil AB, Robertson BW, Cheney RE. 2006. Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci USA 103(33):12411-12416.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.33 , pp. 12411-12416
    • Bohil, A.B.1    Robertson, B.W.2    Cheney, R.E.3
  • 17
    • 57649133951 scopus 로고    scopus 로고
    • Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge
    • Brzeska H, Hwang KJ, Korn ED. 2008. Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4, 5-bisphosphate at the plasma membrane due to the high concentration of negative charge. J Biol Chem 283(46):32014-32023.
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 32014-32023
    • Brzeska, H.1    Hwang, K.J.2    Korn, E.D.3
  • 20
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone KG, Welch MD. 2010. A nucleator arms race: cellular control of actin assembly. Nat Rev Mol Cell Biol 11(4):237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 21
    • 84905279377 scopus 로고    scopus 로고
    • Elevated expression of myosin X in tumours contributes to breast cancer aggressiveness and metastasis
    • Cao R, Chen J, Zhang X, Zhai Y, Qing X, Xing W, Zhang L, Malik YS, Yu H, Zhu X. 2014. Elevated expression of myosin X in tumours contributes to breast cancer aggressiveness and metastasis. Br J Cancer 111(3):539-550.
    • (2014) Br J Cancer , vol.111 , Issue.3 , pp. 539-550
    • Cao, R.1    Chen, J.2    Zhang, X.3    Zhai, Y.4    Qing, X.5    Xing, W.6    Zhang, L.7    Malik, Y.S.8    Yu, H.9    Zhu, X.10
  • 22
    • 84867400931 scopus 로고    scopus 로고
    • Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres
    • Cervero P, Himmel M, Kruger M, Linder S. 2012. Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres. Eur J Cell Biol 91(11-12):908-922.
    • (2012) Eur J Cell Biol , vol.91 , Issue.11-12 , pp. 908-922
    • Cervero, P.1    Himmel, M.2    Kruger, M.3    Linder, S.4
  • 23
    • 84863516735 scopus 로고    scopus 로고
    • A role for myosin IXb, a motor-RhoGAP chimera, in epithelial wound healing and tight junction regulation
    • Chandhoke SK, Mooseker MS. 2012. A role for myosin IXb, a motor-RhoGAP chimera, in epithelial wound healing and tight junction regulation. Mol Biol Cell 23(13):2468-2480.
    • (2012) Mol Biol Cell , vol.23 , Issue.13 , pp. 2468-2480
    • Chandhoke, S.K.1    Mooseker, M.S.2
  • 24
    • 84864743481 scopus 로고    scopus 로고
    • Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis
    • Cheng J, Grassart A, Drubin DG. 2012. Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis. Mol Biol Cell 23(15):2891-2904.
    • (2012) Mol Biol Cell , vol.23 , Issue.15 , pp. 2891-2904
    • Cheng, J.1    Grassart, A.2    Drubin, D.G.3
  • 25
    • 77956480550 scopus 로고    scopus 로고
    • Myosin VI and optineurin are required for polarized EGFR delivery and directed migration
    • Chibalina MV, Poliakov A, Kendrick-Jones J, Buss F. 2010. Myosin VI and optineurin are required for polarized EGFR delivery and directed migration. Traffic 11(10):1290-1303.
    • (2010) Traffic , vol.11 , Issue.10 , pp. 1290-1303
    • Chibalina, M.V.1    Poliakov, A.2    Kendrick-Jones, J.3    Buss, F.4
  • 26
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • Conti MA, Even-Ram S, Liu C, Yamada KM, Adelstein RS. 2004. Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J Biol Chem 279(40):41263-41266.
    • (2004) J Biol Chem , vol.279 , Issue.40 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 30
    • 84863617167 scopus 로고    scopus 로고
    • Inactivation of MYO5B promotes invasion and motility in gastric cancer cells
    • Dong W, Chen X, Chen P, Yue D, Zhu L, Fan Q. 2012. Inactivation of MYO5B promotes invasion and motility in gastric cancer cells. Dig Dis Sci 57(5):1247-1252.
    • (2012) Dig Dis Sci , vol.57 , Issue.5 , pp. 1247-1252
    • Dong, W.1    Chen, X.2    Chen, P.3    Yue, D.4    Zhu, L.5    Fan, Q.6
  • 33
    • 84862833208 scopus 로고    scopus 로고
    • Targeting invadopodia to block breast cancer metastasis
    • Eckert MA, Yang J. 2011. Targeting invadopodia to block breast cancer metastasis. Oncotarget 2(7):562-568.
    • (2011) Oncotarget , vol.2 , Issue.7 , pp. 562-568
    • Eckert, M.A.1    Yang, J.2
  • 36
    • 41649121862 scopus 로고    scopus 로고
    • Collective epithelial migration and cell rearrangements drive mammary branching morphogenesis
    • Ewald AJ, Brenot A, Duong M, Chan BS, Werb Z. 2008. Collective epithelial migration and cell rearrangements drive mammary branching morphogenesis. Dev Cell 14(4):570-581.
    • (2008) Dev Cell , vol.14 , Issue.4 , pp. 570-581
    • Ewald, A.J.1    Brenot, A.2    Duong, M.3    Chan, B.S.4    Werb, Z.5
  • 37
    • 79952830155 scopus 로고    scopus 로고
    • Shroom2 regulates contractility to control endothelial morphogenesis
    • Farber MJ, Rizaldy R, Hildebrand JD. 2011. Shroom2 regulates contractility to control endothelial morphogenesis. Mol Biol Cell 22(6):795-805.
    • (2011) Mol Biol Cell , vol.22 , Issue.6 , pp. 795-805
    • Farber, M.J.1    Rizaldy, R.2    Hildebrand, J.D.3
  • 39
    • 78049263512 scopus 로고    scopus 로고
    • Myo1e binds anionic phospholipids with high affinity
    • Feeser EA, Ignacio CM, Krendel M, Ostap EM. 2010. Myo1e binds anionic phospholipids with high affinity. Biochemistry 49(43):9353-9360.
    • (2010) Biochemistry , vol.49 , Issue.43 , pp. 9353-9360
    • Feeser, E.A.1    Ignacio, C.M.2    Krendel, M.3    Ostap, E.M.4
  • 41
    • 59549090911 scopus 로고    scopus 로고
    • Local cortical tension by myosin II guides 3D endothelial cell branching
    • Fischer RS, Gardel M, Ma X, Adelstein RS, Waterman CM. 2009. Local cortical tension by myosin II guides 3D endothelial cell branching. Curr Biol 19(3):260-265.
    • (2009) Curr Biol , vol.19 , Issue.3 , pp. 260-265
    • Fischer, R.S.1    Gardel, M.2    Ma, X.3    Adelstein, R.S.4    Waterman, C.M.5
  • 42
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth BJ, Goedecke MC, Soldati D. 2006. New insights into myosin evolution and classification. Proc Natl Acad Sci USA 103(10):3681-3686.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.10 , pp. 3681-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 43
    • 67649528138 scopus 로고    scopus 로고
    • Collective cell migration in morphogenesis, regeneration and cancer
    • Friedl P, Gilmour D. 2009. Collective cell migration in morphogenesis, regeneration and cancer. Nat Rev Mol Cell Biol 10(7):445-457.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.7 , pp. 445-457
    • Friedl, P.1    Gilmour, D.2
  • 44
    • 84864886120 scopus 로고    scopus 로고
    • Classifying collective cancer cell invasion
    • Friedl P, Locker J, Sahai E, Segall JE. 2012. Classifying collective cancer cell invasion. Nat Cell Biol 14(8):777-783.
    • (2012) Nat Cell Biol , vol.14 , Issue.8 , pp. 777-783
    • Friedl, P.1    Locker, J.2    Sahai, E.3    Segall, J.E.4
  • 45
    • 0024848148 scopus 로고
    • Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family
    • Garcia A, Coudrier E, Carboni J, Anderson J, Vandekerkhove J, Mooseker M, Louvard D, Arpin M. 1989. Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family. J Cell Biol 109(6 Pt 1):2895-2903.
    • (1989) J Cell Biol , vol.109 , Issue.6 , pp. 2895-2903
    • Garcia, A.1    Coudrier, E.2    Carboni, J.3    Anderson, J.4    Vandekerkhove, J.5    Mooseker, M.6    Louvard, D.7    Arpin, M.8
  • 46
    • 0036052866 scopus 로고    scopus 로고
    • Myosin VI is required for E-cadherin-mediated border cell migration
    • Geisbrecht ER, Montell DJ. 2002. Myosin VI is required for E-cadherin-mediated border cell migration. Nat Cell Biol 4(8):616-620.
    • (2002) Nat Cell Biol , vol.4 , Issue.8 , pp. 616-620
    • Geisbrecht, E.R.1    Montell, D.J.2
  • 47
    • 84872845163 scopus 로고    scopus 로고
    • Regulation and control of myosin-I by the motor and light chain-binding domains
    • Greenberg MJ, Ostap EM. 2013. Regulation and control of myosin-I by the motor and light chain-binding domains. Trends Cell Biol 23(2):81-89.
    • (2013) Trends Cell Biol , vol.23 , Issue.2 , pp. 81-89
    • Greenberg, M.J.1    Ostap, E.M.2
  • 48
    • 77950346282 scopus 로고    scopus 로고
    • Immunity, inflammation, and cancer
    • Grivennikov SI, Greten FR, Karin M. 2010. Immunity, inflammation, and cancer. Cell 140(6):883-899.
    • (2010) Cell , vol.140 , Issue.6 , pp. 883-899
    • Grivennikov, S.I.1    Greten, F.R.2    Karin, M.3
  • 49
    • 79958726446 scopus 로고    scopus 로고
    • Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties
    • Guzik-Lendrum S, Nagy A, Takagi Y, Houdusse A, Sellers JR. 2011. Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties. J Biol Chem 286(24):21755-21766.
    • (2011) J Biol Chem , vol.286 , Issue.24 , pp. 21755-21766
    • Guzik-Lendrum, S.1    Nagy, A.2    Takagi, Y.3    Houdusse, A.4    Sellers, J.R.5
  • 50
    • 84875162359 scopus 로고    scopus 로고
    • A gene signature for predicting outcome in patients with basal-like breast cancer
    • Hallett RM, Dvorkin-Gheva A, Bane A, Hassell JA. 2012. A gene signature for predicting outcome in patients with basal-like breast cancer. Sci Rep 2:227.
    • (2012) Sci Rep , vol.2 , pp. 227
    • Hallett, R.M.1    Dvorkin-Gheva, A.2    Bane, A.3    Hassell, J.A.4
  • 51
    • 84355161386 scopus 로고    scopus 로고
    • Walking to work: roles for class V myosins as cargo transporters
    • Hammer JA, III, Sellers JR. 2012. Walking to work: roles for class V myosins as cargo transporters. Nat Rev Mol Cell Biol 13(1):13-26.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.1 , pp. 13-26
    • Hammer III, J.A.1    Sellers, J.R.2
  • 52
    • 84885142879 scopus 로고    scopus 로고
    • Functions of class V myosins in neurons
    • Hammer JA, III, Wagner W. 2013. Functions of class V myosins in neurons. J Biol Chem 288(40):28428-28434.
    • (2013) J Biol Chem , vol.288 , Issue.40 , pp. 28428-28434
    • Hammer III, J.A.1    Wagner, W.2
  • 53
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D, Weinberg RA. 2011. Hallmarks of cancer: the next generation. Cell 144(5):646-674.
    • (2011) Cell , vol.144 , Issue.5 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 54
    • 84855551714 scopus 로고    scopus 로고
    • Links between mutant p53 and genomic instability
    • Hanel W, Moll UM. 2012. Links between mutant p53 and genomic instability. J Cell Biochem 113(2):433-439.
    • (2012) J Cell Biochem , vol.113 , Issue.2 , pp. 433-439
    • Hanel, W.1    Moll, U.M.2
  • 55
    • 84863104644 scopus 로고    scopus 로고
    • The myosin superfamily at a glance
    • Hartman MA, Spudich JA. 2012. The myosin superfamily at a glance. J Cell Sci 125(Pt 7):1627-1632.
    • (2012) J Cell Sci 125(Pt , vol.7 , pp. 1627-1632
    • Hartman, M.A.1    Spudich, J.A.2
  • 57
    • 33750515229 scopus 로고    scopus 로고
    • Myo1c binds phosphoinositides through a putative pleckstrin homology domain
    • Hokanson DE, Laakso JM, Lin T, Sept D, Ostap EM. 2006. Myo1c binds phosphoinositides through a putative pleckstrin homology domain. Mol Biol Cell 17(11):4856-4865.
    • (2006) Mol Biol Cell , vol.17 , Issue.11 , pp. 4856-4865
    • Hokanson, D.E.1    Laakso, J.M.2    Lin, T.3    Sept, D.4    Ostap, E.M.5
  • 58
    • 75649094184 scopus 로고    scopus 로고
    • Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration
    • Hsu RM, Tsai MH, Hsieh YJ, Lyu PC, Yu JS. 2010. Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration. Mol Biol Cell 21(2):287-301.
    • (2010) Mol Biol Cell , vol.21 , Issue.2 , pp. 287-301
    • Hsu, R.M.1    Tsai, M.H.2    Hsieh, Y.J.3    Lyu, P.C.4    Yu, J.S.5
  • 60
    • 76049106434 scopus 로고    scopus 로고
    • Polarity protein alterations in carcinoma: a focus on emerging roles for polarity regulators
    • Huang L, Muthuswamy SK. 2010. Polarity protein alterations in carcinoma: a focus on emerging roles for polarity regulators. Curr Opin Genet Dev 20(1):41-50.
    • (2010) Curr Opin Genet Dev , vol.20 , Issue.1 , pp. 41-50
    • Huang, L.1    Muthuswamy, S.K.2
  • 63
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • Kelley CA, Sellers JR, Gard DL, Bui D, Adelstein RS, Baines IC. 1996. Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities. J Cell Biol 134(3):675-687.
    • (1996) J Cell Biol , vol.134 , Issue.3 , pp. 675-687
    • Kelley, C.A.1    Sellers, J.R.2    Gard, D.L.3    Bui, D.4    Adelstein, R.S.5    Baines, I.C.6
  • 64
    • 84856777960 scopus 로고    scopus 로고
    • Myosin-X: a MyTH-FERM myosin at the tips of filopodia
    • Kerber ML, Cheney RE. 2011. Myosin-X: a MyTH-FERM myosin at the tips of filopodia. J Cell Sci 124(Pt 22):3733-3741.
    • (2011) J Cell Sci , vol.124 , pp. 3733-3741
    • Kerber, M.L.1    Cheney, R.E.2
  • 65
    • 34047220868 scopus 로고    scopus 로고
    • Cancer immunoediting from immune surveillance to immune escape
    • Kim R, Emi M, Tanabe K. 2007. Cancer immunoediting from immune surveillance to immune escape. Immunology 121(1):1-14.
    • (2007) Immunology , vol.121 , Issue.1 , pp. 1-14
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 67
    • 0031711721 scopus 로고    scopus 로고
    • Cytoplasmic dynamics of myosin IIA and IIB: spatial 'sorting' of isoforms in locomoting cells
    • Kolega J. 1998. Cytoplasmic dynamics of myosin IIA and IIB: spatial 'sorting' of isoforms in locomoting cells. J Cell Sci 111(Pt 15):2085-2095.
    • (1998) J Cell Sci , vol.111 , pp. 2085-2095
    • Kolega, J.1
  • 68
    • 84863865683 scopus 로고    scopus 로고
    • Myosin Ia is required for CFTR brush border membrane trafficking and ion transport in the mouse small intestine
    • Kravtsov DV, Caputo C, Collaco A, Hoekstra N, Egan ME, Mooseker MS, Ameen NA. 2012. Myosin Ia is required for CFTR brush border membrane trafficking and ion transport in the mouse small intestine. Traffic 13(8):1072-1082.
    • (2012) Traffic , vol.13 , Issue.8 , pp. 1072-1082
    • Kravtsov, D.V.1    Caputo, C.2    Collaco, A.3    Hoekstra, N.4    Egan, M.E.5    Mooseker, M.S.6    Ameen, N.A.7
  • 69
    • 24044500344 scopus 로고    scopus 로고
    • Myosins: tails (and heads) of functional diversity
    • Krendel M, Mooseker MS. 2005. Myosins: tails (and heads) of functional diversity. Physiology (Bethesda) 20:239-251.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 70
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • Krendel M, Osterweil EK, Mooseker MS. 2007. Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett 581(4):644-650.
    • (2007) FEBS Lett , vol.581 , Issue.4 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 72
    • 73449131219 scopus 로고    scopus 로고
    • Upregulation of myosin Va by Snail is involved in cancer cell migration and metastasis
    • Lan L, Han H, Zuo H, Chen Z, Du Y, Zhao W, Gu J, Zhang Z. 2010. Upregulation of myosin Va by Snail is involved in cancer cell migration and metastasis. Int J Cancer 126(1):53-64.
    • (2010) Int J Cancer , vol.126 , Issue.1 , pp. 53-64
    • Lan, L.1    Han, H.2    Zuo, H.3    Chen, Z.4    Du, Y.5    Zhao, W.6    Gu, J.7    Zhang, Z.8
  • 73
    • 33744931917 scopus 로고    scopus 로고
    • The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA
    • Li ZH, Bresnick AR. 2006. The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA. Cancer Res 66(10):5173-5180.
    • (2006) Cancer Res , vol.66 , Issue.10 , pp. 5173-5180
    • Li, Z.H.1    Bresnick, A.R.2
  • 74
    • 80054031825 scopus 로고    scopus 로고
    • Degrading devices: invadosomes in proteolytic cell invasion
    • Linder S, Wiesner C, Himmel M. 2011. Degrading devices: invadosomes in proteolytic cell invasion. Annu Rev Cell Dev Biol 27:185-211.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 185-211
    • Linder, S.1    Wiesner, C.2    Himmel, M.3
  • 76
    • 34250351476 scopus 로고    scopus 로고
    • Loss of cell adhesion causes hydrocephalus in nonmuscle myosin II-B-ablated and mutated mice
    • Ma X, Bao J, Adelstein RS. 2007. Loss of cell adhesion causes hydrocephalus in nonmuscle myosin II-B-ablated and mutated mice. Mol Biol Cell 18(6):2305-2312.
    • (2007) Mol Biol Cell , vol.18 , Issue.6 , pp. 2305-2312
    • Ma, X.1    Bao, J.2    Adelstein, R.S.3
  • 77
    • 34547591456 scopus 로고    scopus 로고
    • Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell cell contacts in mammalian epithelial cells
    • Maddugoda MP, Crampton MS, Shewan AM, Yap AS. 2007. Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell cell contacts in mammalian epithelial cells. J Cell Biol 178(3):529-540.
    • (2007) J Cell Biol , vol.178 , Issue.3 , pp. 529-540
    • Maddugoda, M.P.1    Crampton, M.S.2    Shewan, A.M.3    Yap, A.S.4
  • 78
    • 0035901599 scopus 로고    scopus 로고
    • Cell adhesion: ushering in a new understanding of myosin VII
    • Maniak M. 2001. Cell adhesion: ushering in a new understanding of myosin VII. Curr Biol 11(8):R315-R317.
    • (2001) Curr Biol , vol.11 , Issue.8 , pp. R315-R317
    • Maniak, M.1
  • 79
    • 84855337379 scopus 로고    scopus 로고
    • The myosin family: unconventional roles of actin-dependent molecular motors in immune cells
    • Maravillas-Montero JL, Santos-Argumedo L. 2012. The myosin family: unconventional roles of actin-dependent molecular motors in immune cells. J Leukoc Biol 91(1):35-46.
    • (2012) J Leukoc Biol , vol.91 , Issue.1 , pp. 35-46
    • Maravillas-Montero, J.L.1    Santos-Argumedo, L.2
  • 81
    • 0027999246 scopus 로고
    • Differential localization of myosin-II isozymes in human cultured cells and blood cells
    • Maupin P, Phillips CL, Adelstein RS, Pollard TD. 1994. Differential localization of myosin-II isozymes in human cultured cells and blood cells. J Cell Sci 107(Pt 11):3077-3090.
    • (1994) J Cell Sci , vol.107 , pp. 3077-3090
    • Maupin, P.1    Phillips, C.L.2    Adelstein, R.S.3    Pollard, T.D.4
  • 82
    • 84859740875 scopus 로고    scopus 로고
    • Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain
    • Mazerik JN, Tyska MJ. 2012. Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain. J Biol Chem 287(16):13104-13115.
    • (2012) J Biol Chem , vol.287 , Issue.16 , pp. 13104-13115
    • Mazerik, J.N.1    Tyska, M.J.2
  • 85
    • 34249098669 scopus 로고    scopus 로고
    • Myosin-1a powers the sliding of apical membrane along microvillar actin bundles
    • McConnell RE, Tyska MJ. 2007. Myosin-1a powers the sliding of apical membrane along microvillar actin bundles. J Cell Biol 177(4):671-681.
    • (2007) J Cell Biol , vol.177 , Issue.4 , pp. 671-681
    • McConnell, R.E.1    Tyska, M.J.2
  • 86
    • 77954315036 scopus 로고    scopus 로고
    • Leveraging the membrane-cytoskeleton interface with myosin-1
    • McConnell RE, Tyska MJ. 2010. Leveraging the membrane-cytoskeleton interface with myosin-1. Trends Cell Biol 20(7):418-426.
    • (2010) Trends Cell Biol , vol.20 , Issue.7 , pp. 418-426
    • McConnell, R.E.1    Tyska, M.J.2
  • 89
    • 84876705952 scopus 로고    scopus 로고
    • The regulation and functional impact of actin assembly at cadherin cell-cell adhesions
    • Michael M, Yap AS. 2013. The regulation and functional impact of actin assembly at cadherin cell-cell adhesions. Semin Cell Dev Biol 24(4):298-307.
    • (2013) Semin Cell Dev Biol , vol.24 , Issue.4 , pp. 298-307
    • Michael, M.1    Yap, A.S.2
  • 90
    • 84875373346 scopus 로고    scopus 로고
    • Physical break-down of the classical view on cancer cell invasion and metastasis
    • Mierke CT. 2013. Physical break-down of the classical view on cancer cell invasion and metastasis. Eur J Cell Biol 92(3):89-104.
    • (2013) Eur J Cell Biol , vol.92 , Issue.3 , pp. 89-104
    • Mierke, C.T.1
  • 92
    • 0024312342 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme
    • Mooseker MS, Coleman TR. 1989. The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme. J Cell Biol 108(6):2395-2400.
    • (1989) J Cell Biol , vol.108 , Issue.6 , pp. 2395-2400
    • Mooseker, M.S.1    Coleman, T.R.2
  • 93
    • 0039521743 scopus 로고    scopus 로고
    • The rat myosin myr 5 is a GTPase-activating protein for Rho in vivo: essential role of arginine 1695
    • Muller RT, Honnert U, Reinhard J, Bahler M. 1997. The rat myosin myr 5 is a GTPase-activating protein for Rho in vivo: essential role of arginine 1695. Mol Biol Cell 8(10):2039-2053.
    • (1997) Mol Biol Cell , vol.8 , Issue.10 , pp. 2039-2053
    • Muller, R.T.1    Honnert, U.2    Reinhard, J.3    Bahler, M.4
  • 94
    • 17644367505 scopus 로고    scopus 로고
    • Genetic and epigenetic alterations of the candidate tumor-suppressor gene MYO18B, on chromosome arm 22q, in colorectal cancer
    • Nakano T, Tani M, Nishioka M, Kohno T, Otsuka A, Ohwada S, Yokota J. 2005. Genetic and epigenetic alterations of the candidate tumor-suppressor gene MYO18B, on chromosome arm 22q, in colorectal cancer. Genes Chromosomes Cancer 43(2):162-171.
    • (2005) Genes Chromosomes Cancer , vol.43 , Issue.2 , pp. 162-171
    • Nakano, T.1    Tani, M.2    Nishioka, M.3    Kohno, T.4    Otsuka, A.5    Ohwada, S.6    Yokota, J.7
  • 95
    • 33748940402 scopus 로고    scopus 로고
    • Role of angiogenesis in human tumor dormancy: animal models of the angiogenic switch
    • Naumov GN, Akslen LA, Folkman J. 2006. Role of angiogenesis in human tumor dormancy: animal models of the angiogenic switch. Cell Cycle 5(16):1779-1787.
    • (2006) Cell Cycle , vol.5 , Issue.16 , pp. 1779-1787
    • Naumov, G.N.1    Akslen, L.A.2    Folkman, J.3
  • 97
    • 34247606028 scopus 로고    scopus 로고
    • Myosin at work: motor adaptations for a variety of cellular functions
    • O'Connell CB, Tyska MJ, Mooseker MS. 2007. Myosin at work: motor adaptations for a variety of cellular functions. Biochim Biophys Acta 1773(5):615-630.
    • (2007) Biochim Biophys Acta , vol.1773 , Issue.5 , pp. 615-630
    • O'Connell, C.B.1    Tyska, M.J.2    Mooseker, M.S.3
  • 98
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species
    • Odronitz F, Kollmar M. 2007. Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species. Genome Biol 8(9):R196.
    • (2007) Genome Biol , vol.8 , Issue.9 , pp. R196
    • Odronitz, F.1    Kollmar, M.2
  • 99
    • 77955363995 scopus 로고    scopus 로고
    • TP53 mutations in human cancers: origins, consequences, and clinical use
    • Olivier M, Hollstein M, Hainaut P. 2010. TP53 mutations in human cancers: origins, consequences, and clinical use. Cold Spring Harb Perspect Biol 2(1):a001008.
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , Issue.1 , pp. a001008
    • Olivier, M.1    Hollstein, M.2    Hainaut, P.3
  • 100
    • 84857345144 scopus 로고    scopus 로고
    • Myosin-IXA regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions
    • Omelchenko T, Hall A. 2012. Myosin-IXA regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Curr Biol 22(4):278-288.
    • (2012) Curr Biol , vol.22 , Issue.4 , pp. 278-288
    • Omelchenko, T.1    Hall, A.2
  • 101
    • 60849138840 scopus 로고    scopus 로고
    • Tropomyosins as discriminators of myosin function
    • Ostap EM. 2008. Tropomyosins as discriminators of myosin function. Adv Exp Med Biol 644:273-282.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 273-282
    • Ostap, E.M.1
  • 102
    • 84896054853 scopus 로고    scopus 로고
    • Myosin 1e is a component of the invadosome core that contributes to regulation of invadosome dynamics
    • Ouderkirk JL, Krendel M. 2014. Myosin 1e is a component of the invadosome core that contributes to regulation of invadosome dynamics. Exp Cell Res 322(2):265-276.
    • (2014) Exp Cell Res , vol.322 , Issue.2 , pp. 265-276
    • Ouderkirk, J.L.1    Krendel, M.2
  • 103
    • 77950573946 scopus 로고    scopus 로고
    • Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)
    • Patino-Lopez G, Aravind L, Dong X, Kruhlak MJ, Ostap EM, Shaw S. 2010. Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH). J Biol Chem 285(12):8675-8686.
    • (2010) J Biol Chem , vol.285 , Issue.12 , pp. 8675-8686
    • Patino-Lopez, G.1    Aravind, L.2    Dong, X.3    Kruhlak, M.J.4    Ostap, E.M.5    Shaw, S.6
  • 104
    • 38049037417 scopus 로고    scopus 로고
    • Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors
    • Pi X, Ren R, Kelley R, Zhang C, Moser M, Bohil AB, Divito M, Cheney RE, Patterson C. 2007. Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors. J Cell Biol 179(7):1569-1582.
    • (2007) J Cell Biol , vol.179 , Issue.7 , pp. 1569-1582
    • Pi, X.1    Ren, R.2    Kelley, R.3    Zhang, C.4    Moser, M.5    Bohil, A.B.6    Divito, M.7    Cheney, R.E.8    Patterson, C.9
  • 105
    • 84908028943 scopus 로고    scopus 로고
    • Getting myosin-V on the right track: tropomyosin sorts transport in yeast
    • Pollard LW, Lord M. 2014. Getting myosin-V on the right track: tropomyosin sorts transport in yeast. Bioarchitecture 4(1):35-38.
    • (2014) Bioarchitecture , vol.4 , Issue.1 , pp. 35-38
    • Pollard, L.W.1    Lord, M.2
  • 106
    • 0031977198 scopus 로고    scopus 로고
    • Human myosin-IXb is a mechanochemically active motor and a GAP for rho
    • Post PL, Bokoch GM, Mooseker MS. 1998. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. J Cell Sci 111(Pt 7):941-950.
    • (1998) J Cell Sci , vol.111 , pp. 941-950
    • Post, P.L.1    Bokoch, G.M.2    Mooseker, M.S.3
  • 107
    • 60849087095 scopus 로고    scopus 로고
    • Tropomyosin function in yeast
    • Pruyne D. 2008. Tropomyosin function in yeast. Adv Exp Med Biol 644:168-186.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 168-186
    • Pruyne, D.1
  • 108
    • 74449085968 scopus 로고    scopus 로고
    • Overexpression of myosin VI in prostate cancer cells enhances PSA and VEGF secretion, but has no effect on endocytosis
    • Puri C, Chibalina MV, Arden SD, Kruppa AJ, Kendrick-Jones J, Buss F. 2010. Overexpression of myosin VI in prostate cancer cells enhances PSA and VEGF secretion, but has no effect on endocytosis. Oncogene 29(2):188-200.
    • (2010) Oncogene , vol.29 , Issue.2 , pp. 188-200
    • Puri, C.1    Chibalina, M.V.2    Arden, S.D.3    Kruppa, A.J.4    Kendrick-Jones, J.5    Buss, F.6
  • 109
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A. 2001. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293(5536):1829-1832.
    • (2001) Science , vol.293 , Issue.5536 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 110
    • 45149094267 scopus 로고    scopus 로고
    • Basal-like breast cancer: a critical review
    • Rakha EA, Reis-Filho JS, Ellis IO. 2008. Basal-like breast cancer: a critical review. J Clin Oncol 26(15):2568-2581.
    • (2008) J Clin Oncol , vol.26 , Issue.15 , pp. 2568-2581
    • Rakha, E.A.1    Reis-Filho, J.S.2    Ellis, I.O.3
  • 111
    • 24144503755 scopus 로고    scopus 로고
    • Myosin domain evolution and the primary divergence of eukaryotes
    • Richards TA, Cavalier-Smith T. 2005. Myosin domain evolution and the primary divergence of eukaryotes. Nature 436(7054):1113-1118.
    • (2005) Nature , vol.436 , Issue.7054 , pp. 1113-1118
    • Richards, T.A.1    Cavalier-Smith, T.2
  • 112
    • 0035853701 scopus 로고    scopus 로고
    • The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X
    • Rogers MS, Strehler EE. 2001. The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X. J Biol Chem 276(15):12182-12189.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 12182-12189
    • Rogers, M.S.1    Strehler, E.E.2
  • 113
    • 80051724097 scopus 로고    scopus 로고
    • Epithelial cell polarity: a major gatekeeper against cancer?
    • Royer C, Lu X. 2011. Epithelial cell polarity: a major gatekeeper against cancer? Cell Death Differ 18(9):1470-1477.
    • (2011) Cell Death Differ , vol.18 , Issue.9 , pp. 1470-1477
    • Royer, C.1    Lu, X.2
  • 114
    • 12344252751 scopus 로고    scopus 로고
    • Mechanisms of cancer cell invasion
    • Sahai E. 2005. Mechanisms of cancer cell invasion. Curr Opin Genet Dev 15(1):87-96.
    • (2005) Curr Opin Genet Dev , vol.15 , Issue.1 , pp. 87-96
    • Sahai, E.1
  • 115
    • 33845993635 scopus 로고    scopus 로고
    • Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration
    • Sandquist JC, Swenson KI, Demali KA, Burridge K, Means AR. 2006. Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration. J Biol Chem 281(47):35873-35883.
    • (2006) J Biol Chem , vol.281 , Issue.47 , pp. 35873-35883
    • Sandquist, J.C.1    Swenson, K.I.2    Demali, K.A.3    Burridge, K.4    Means, A.R.5
  • 116
    • 79952283069 scopus 로고    scopus 로고
    • Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins
    • Schiller HB, Friedel CC, Boulegue C, Fassler R. 2011. Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins. EMBO Rep 12(3):259-266.
    • (2011) EMBO Rep , vol.12 , Issue.3 , pp. 259-266
    • Schiller, H.B.1    Friedel, C.C.2    Boulegue, C.3    Fassler, R.4
  • 117
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM. 2010. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J Cell Biol 189(3):541-556.
    • (2010) J Cell Biol , vol.189 , Issue.3 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 118
    • 84892594373 scopus 로고    scopus 로고
    • Direct in vivo RNAi screen unveils myosin IIa as a tumor suppressor of squamous cell carcinomas
    • Schramek D, Sendoel A, Segal JP, Beronja S, Heller E, Oristian D, Reva B, Fuchs E. 2014. Direct in vivo RNAi screen unveils myosin IIa as a tumor suppressor of squamous cell carcinomas. Science 343(6168):309-313.
    • (2014) Science , vol.343 , Issue.6168 , pp. 309-313
    • Schramek, D.1    Sendoel, A.2    Segal, J.P.3    Beronja, S.4    Heller, E.5    Oristian, D.6    Reva, B.7    Fuchs, E.8
  • 120
    • 84866242179 scopus 로고    scopus 로고
    • The outgrowth of micrometastases is enabled by the formation of filopodium-like protrusions
    • Shibue T, Brooks MW, Inan MF, Reinhardt F, Weinberg RA. 2012. The outgrowth of micrometastases is enabled by the formation of filopodium-like protrusions. Cancer Discov 2(8):706-721.
    • (2012) Cancer Discov , vol.2 , Issue.8 , pp. 706-721
    • Shibue, T.1    Brooks, M.W.2    Inan, M.F.3    Reinhardt, F.4    Weinberg, R.A.5
  • 121
    • 84867400312 scopus 로고    scopus 로고
    • Invadopodia: the leading force
    • Sibony-Benyamini H, Gil-Henn H. 2012. Invadopodia: the leading force. Eur J Cell Biol 91(11-12):896-901.
    • (2012) Eur J Cell Biol , vol.91 , Issue.11-12 , pp. 896-901
    • Sibony-Benyamini, H.1    Gil-Henn, H.2
  • 122
    • 0032459354 scopus 로고    scopus 로고
    • Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells
    • Skowron JF, Bement WM, Mooseker MS. 1998. Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells. Cell Motil Cytoskeleton 41(4):308-324.
    • (1998) Cell Motil Cytoskeleton , vol.41 , Issue.4 , pp. 308-324
    • Skowron, J.F.1    Bement, W.M.2    Mooseker, M.S.3
  • 123
    • 67650770689 scopus 로고    scopus 로고
    • The molecular biology of mixed lineage leukemia
    • Slany RK. 2009. The molecular biology of mixed lineage leukemia. Haematologica 94(7):984-993.
    • (2009) Haematologica , vol.94 , Issue.7 , pp. 984-993
    • Slany, R.K.1
  • 124
    • 25844435342 scopus 로고    scopus 로고
    • Myosin-X: a molecular motor at the cell's fingertips
    • Sousa AD, Cheney RE. 2005. Myosin-X: a molecular motor at the cell's fingertips. Trends Cell Biol 15(10):533-539.
    • (2005) Trends Cell Biol , vol.15 , Issue.10 , pp. 533-539
    • Sousa, A.D.1    Cheney, R.E.2
  • 125
    • 77949457529 scopus 로고    scopus 로고
    • Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast
    • Stark BC, Sladewski TE, Pollard LW, Lord M. 2010. Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast. Mol Biol Cell 21(6):989-1000.
    • (2010) Mol Biol Cell , vol.21 , Issue.6 , pp. 989-1000
    • Stark, B.C.1    Sladewski, T.E.2    Pollard, L.W.3    Lord, M.4
  • 126
    • 2942679778 scopus 로고    scopus 로고
    • The early history of the biochemistry of muscle contraction
    • Szent-Gyorgyi AG. 2004. The early history of the biochemistry of muscle contraction. J Gen Physiol 123(6):631-641.
    • (2004) J Gen Physiol , vol.123 , Issue.6 , pp. 631-641
    • Szent-Gyorgyi, A.G.1
  • 127
    • 84886892623 scopus 로고    scopus 로고
    • Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3
    • Taft MH, Behrmann E, Munske-Weidemann LC, Thiel C, Raunser S, Manstein DJ. 2013. Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3. J Biol Chem 288(42):30029-30041.
    • (2013) J Biol Chem , vol.288 , Issue.42 , pp. 30029-30041
    • Taft, M.H.1    Behrmann, E.2    Munske-Weidemann, L.C.3    Thiel, C.4    Raunser, S.5    Manstein, D.J.6
  • 128
    • 23444443669 scopus 로고    scopus 로고
    • The MYO1F, unconventional myosin type 1F, gene is fused to MLL in infant acute monocytic leukemia with a complex translocation involving chromosomes 7, 11, 19 and 22
    • Taki T, Akiyama M, Saito S, Ono R, Taniwaki M, Kato Y, Yuza Y, Eto Y, Hayashi Y. 2005. The MYO1F, unconventional myosin type 1F, gene is fused to MLL in infant acute monocytic leukemia with a complex translocation involving chromosomes 7, 11, 19 and 22. Oncogene 24(33):5191-5197.
    • (2005) Oncogene , vol.24 , Issue.33 , pp. 5191-5197
    • Taki, T.1    Akiyama, M.2    Saito, S.3    Ono, R.4    Taniwaki, M.5    Kato, Y.6    Yuza, Y.7    Eto, Y.8    Hayashi, Y.9
  • 130
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery JP. 2002. Epithelial-mesenchymal transitions in tumour progression. Nat Rev Cancer 2(6):442-454.
    • (2002) Nat Rev Cancer , vol.2 , Issue.6 , pp. 442-454
    • Thiery, J.P.1
  • 131
    • 84874599441 scopus 로고    scopus 로고
    • The myosin motor Myo1c is required for VEGFR2 delivery to the cell surface and for angiogenic signaling
    • Tiwari A, Jung JJ, Inamdar SM, Nihalani D, Choudhury A. 2013. The myosin motor Myo1c is required for VEGFR2 delivery to the cell surface and for angiogenic signaling. Am J Physiol Heart Circ Physiol 304(5):H687-H696.
    • (2013) Am J Physiol Heart Circ Physiol , vol.304 , Issue.5 , pp. H687-H696
    • Tiwari, A.1    Jung, J.J.2    Inamdar, S.M.3    Nihalani, D.4    Choudhury, A.5
  • 133
    • 84884477948 scopus 로고    scopus 로고
    • Myosin-1c regulates the dynamic stability of E-cadherin-based cell-cell contacts in polarized Madin-Darby canine kidney cells
    • Tokuo H, Coluccio LM. 2013. Myosin-1c regulates the dynamic stability of E-cadherin-based cell-cell contacts in polarized Madin-Darby canine kidney cells. Mol Biol Cell 24(18):2820-2833.
    • (2013) Mol Biol Cell , vol.24 , Issue.18 , pp. 2820-2833
    • Tokuo, H.1    Coluccio, L.M.2
  • 134
    • 0036218579 scopus 로고    scopus 로고
    • MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells
    • Tyska MJ, Mooseker MS. 2002. MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. Biophys J 82(4):1869-1883.
    • (2002) Biophys J , vol.82 , Issue.4 , pp. 1869-1883
    • Tyska, M.J.1    Mooseker, M.S.2
  • 135
    • 2442560225 scopus 로고    scopus 로고
    • A role for myosin-1A in the localization of a brush border disaccharidase
    • Tyska MJ, Mooseker MS. 2004. A role for myosin-1A in the localization of a brush border disaccharidase. J Cell Biol 165(3):395-405.
    • (2004) J Cell Biol , vol.165 , Issue.3 , pp. 395-405
    • Tyska, M.J.1    Mooseker, M.S.2
  • 141
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares M, Zareno J, Whitmore L, Choi CK, Horwitz AF. 2007. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J Cell Biol 176(5):573-580.
    • (2007) J Cell Biol , vol.176 , Issue.5 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 142
    • 84890115473 scopus 로고    scopus 로고
    • Cytoskeletal tropomyosins: choreographers of actin filament functional diversity
    • Vindin H, Gunning P. 2013. Cytoskeletal tropomyosins: choreographers of actin filament functional diversity. J Muscle Res Cell Motil 34(3-4):261-274.
    • (2013) J Muscle Res Cell Motil , vol.34 , Issue.3-4 , pp. 261-274
    • Vindin, H.1    Gunning, P.2
  • 143
    • 70349292140 scopus 로고    scopus 로고
    • Colitis-associated cancer: the role of T cells in tumor development
    • Waldner MJ, Neurath MF. 2009. Colitis-associated cancer: the role of T cells in tumor development. Semin Immunopathol 31(2):249-256.
    • (2009) Semin Immunopathol , vol.31 , Issue.2 , pp. 249-256
    • Waldner, M.J.1    Neurath, M.F.2
  • 145
    • 80053367989 scopus 로고    scopus 로고
    • Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains
    • Wang A, Ma X, Conti MA, Adelstein RS. 2011. Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains. Biochem Soc Trans 39(5):1131-1135.
    • (2011) Biochem Soc Trans , vol.39 , Issue.5 , pp. 1131-1135
    • Wang, A.1    Ma, X.2    Conti, M.A.3    Adelstein, R.S.4
  • 146
    • 77955863118 scopus 로고    scopus 로고
    • New insights into the regulation of the actin cytoskeleton by tropomyosin
    • Wang CL, Coluccio LM. 2010. New insights into the regulation of the actin cytoskeleton by tropomyosin. Int Rev Cell Mol Biol 281:91-128.
    • (2010) Int Rev Cell Mol Biol , vol.281 , pp. 91-128
    • Wang, C.L.1    Coluccio, L.M.2
  • 147
    • 80053342176 scopus 로고    scopus 로고
    • The many different cellular functions of MYO7A in the retina
    • Williams DS, Lopes VS. 2011. The many different cellular functions of MYO7A in the retina. Biochem Soc Trans 39(5):1207-1210.
    • (2011) Biochem Soc Trans , vol.39 , Issue.5 , pp. 1207-1210
    • Williams, D.S.1    Lopes, V.S.2
  • 148
    • 0029991890 scopus 로고    scopus 로고
    • Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
    • Wirth JA, Jensen KA, Post PL, Bement WM, Mooseker MS. 1996. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. J Cell Sci 109(Pt 3):653-661.
    • (1996) J Cell Sci , vol.109 , pp. 653-661
    • Wirth, J.A.1    Jensen, K.A.2    Post, P.L.3    Bement, W.M.4    Mooseker, M.S.5
  • 149
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf K, Wu YI, Liu Y, Geiger J, Tam E, Overall C, Stack MS, Friedl P. 2007. Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9(8):893-904.
    • (2007) Nat Cell Biol , vol.9 , Issue.8 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 150
    • 66349129521 scopus 로고    scopus 로고
    • Unconventional myosins acting unconventionally
    • Woolner S, Bement WM. 2009. Unconventional myosins acting unconventionally. Trends Cell Biol 19(6):245-252.
    • (2009) Trends Cell Biol , vol.19 , Issue.6 , pp. 245-252
    • Woolner, S.1    Bement, W.M.2
  • 151
    • 4544283093 scopus 로고    scopus 로고
    • Reduced expression of MYO18B, a candidate tumor-suppressor gene on chromosome arm 22q, in ovarian cancer
    • Yanaihara N, Nishioka M, Kohno T, Otsuka A, Okamoto A, Ochiai K, Tanaka T, Yokota J. 2004. Reduced expression of MYO18B, a candidate tumor-suppressor gene on chromosome arm 22q, in ovarian cancer. Int J Cancer 112(1):150-154.
    • (2004) Int J Cancer , vol.112 , Issue.1 , pp. 150-154
    • Yanaihara, N.1    Nishioka, M.2    Kohno, T.3    Otsuka, A.4    Okamoto, A.5    Ochiai, K.6    Tanaka, T.7    Yokota, J.8
  • 152
    • 80053458405 scopus 로고    scopus 로고
    • Filopodia initiation: focus on the Arp2/3 complex and formins
    • Yang C, Svitkina T. 2011. Filopodia initiation: focus on the Arp2/3 complex and formins. Cell Adh Migr 5(5):402-408.
    • (2011) Cell Adh Migr , vol.5 , Issue.5 , pp. 402-408
    • Yang, C.1    Svitkina, T.2
  • 153
    • 2542623703 scopus 로고    scopus 로고
    • Lessons from border cell migration in the Drosophila ovary: A role for myosin VI in dissemination of human ovarian cancer
    • Yoshida H, Cheng W, Hung J, Montell D, Geisbrecht E, Rosen D, Liu J, Naora H. 2004. Lessons from border cell migration in the Drosophila ovary: A role for myosin VI in dissemination of human ovarian cancer. Proc Natl Acad Sci USA 101(21):8144-8149.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.21 , pp. 8144-8149
    • Yoshida, H.1    Cheng, W.2    Hung, J.3    Montell, D.4    Geisbrecht, E.5    Rosen, D.6    Liu, J.7    Naora, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.